The TatBC complex formation suppresses a modular TatB-multimerization in Escherichia coli.
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Substrate-dependent assembly of the Tat translocase as observed in live Escherichia coli cellsLive cell imaging shows reversible assembly of the TatA component of the twin-arginine protein transport system.Visualizing interactions along the Escherichia coli twin-arginine translocation pathway using protein fragment complementation.Twin-arginine-dependent translocation of folded proteins.The twin-arginine translocation (Tat) protein export pathway.Early contacts between substrate proteins and TatA translocase component in twin-arginine translocation.The TatC component of the twin-arginine protein translocase functions as an obligate oligomer.Initial assembly steps of a translocase for folded proteins.Substrate-triggered position switching of TatA and TatB during Tat transport in Escherichia coli.Following the path of a twin-arginine precursor along the TatABC translocase of Escherichia coliMapping precursor-binding site on TatC subunit of twin arginine-specific protein translocase by site-specific photo cross-linkingProcessing by rhomboid protease is required for Providencia stuartii TatA to interact with TatC and to form functional homo-oligomeric complexes.Recombinant expression of tatABC and tatAC results in the formation of interacting cytoplasmic TatA tubes in Escherichia coli.
P2860
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P2860
The TatBC complex formation suppresses a modular TatB-multimerization in Escherichia coli.
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2007 nî lūn-bûn
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2007年の論文
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name
The TatBC complex formation su ...... erization in Escherichia coli.
@en
The TatBC complex formation su ...... erization in Escherichia coli.
@nl
type
label
The TatBC complex formation su ...... erization in Escherichia coli.
@en
The TatBC complex formation su ...... erization in Escherichia coli.
@nl
prefLabel
The TatBC complex formation su ...... erization in Escherichia coli.
@en
The TatBC complex formation su ...... erization in Escherichia coli.
@nl
P2093
P2860
P1433
P1476
The TatBC complex formation su ...... erization in Escherichia coli.
@en
P2093
Jana Behrendt
Thomas Brüser
Ute Lindenstrauss
P2860
P304
P356
10.1016/J.FEBSLET.2007.07.045
P407
P577
2007-07-30T00:00:00Z